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EC Tree
The expected taxonomic range for this enzyme is: Entamoeba histolytica
Synonyms
ehack, ppi-ehiak, pyrophosphate:acetate phosphotransferase, ppi-dependent ak, ppi-forming acetate kinase,
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acetate kinase (PPi)
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acetate kinase (PPi-forming)
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diphosphate-specific AK
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phosphotransferase, pyrophosphate-acetate
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PPi-forming acetate kinase
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pyrophosphate-acetate phosphotransferase
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-
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pyrophosphate-dependent AK
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pyrophosphate:acetate phosphotransferase
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-
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diphosphate + acetate = phosphate + acetyl phosphate
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phospho group transfer
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diphosphate:acetate phosphotransferase
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acetate + diphosphate
acetyl phosphate + phosphate
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r
acetyl phosphate + phosphate
acetate + diphosphate
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-
-
r
diphosphate + acetate
phosphate + acetyl phosphate
diphosphate + butyrate
phosphate + butyryl phosphate
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-
-
-
?
diphosphate + hexanoate
?
-
-
-
-
?
diphosphate + valerate
phosphate + valeryl phosphate
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-
-
-
?
phosphate + acetyl phosphate
diphosphate + acetate
propionate + acetate
phosphate + propionyl phosphate
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-
-
-
?
additional information
?
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diphosphate + acetate
phosphate + acetyl phosphate
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-
-
-
?
diphosphate + acetate
phosphate + acetyl phosphate
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-
-
-
r
diphosphate + acetate
phosphate + acetyl phosphate
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-
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r
phosphate + acetyl phosphate
diphosphate + acetate
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-
-
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r
phosphate + acetyl phosphate
diphosphate + acetate
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-
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ir
phosphate + acetyl phosphate
diphosphate + acetate
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-
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r
phosphate + acetyl phosphate
diphosphate + acetate
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much greater activity in the direction of acetate formation
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r
phosphate + acetyl phosphate
diphosphate + acetate
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much greater activity in the direction of acetate formation
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r
additional information
?
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no activity with ATP
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-
?
additional information
?
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no activity with ADP, GDP, UDP, IDP or CDP
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-
?
additional information
?
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unlike other characterized ACKs, EhACK shows only diphosphate-dependent activity in the direction of acetyl phosphate formation. ATP does not serve as a phosphoryl donor
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?
additional information
?
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D-glucose 6-phosphate, D-fructose 6-phosphate, D-fructose 1,6-bisphophate, ADP, ATP and AMP used at the physiological concentrations and 1 mM each of 3-phosphoglycerate, 2-phosphoglycerate, phosphoenolpyruvate, UDP-glucose, UTP, O-phosphoserine and phosphocreatine are no substrates for the enzyme. The enzyme has no activity in the acetyl phosphate-forming direction
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additional information
?
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D-glucose 6-phosphate, D-fructose 6-phosphate, D-fructose 1,6-bisphophate, ADP, ATP and AMP used at the physiological concentrations and 1 mM each of 3-phosphoglycerate, 2-phosphoglycerate, phosphoenolpyruvate, UDP-glucose, UTP, O-phosphoserine and phosphocreatine are no substrates for the enzyme. The enzyme has no activity in the acetyl phosphate-forming direction
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additional information
?
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no activity with ADP, GDP, UDP, IDP or CDP
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?
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acetate + diphosphate
acetyl phosphate + phosphate
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-
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r
acetyl phosphate + phosphate
acetate + diphosphate
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-
-
r
diphosphate + acetate
phosphate + acetyl phosphate
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-
-
-
?
phosphate + acetyl phosphate
diphosphate + acetate
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-
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r
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diphosphate
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purified enzyme PPi-ehiAK utilizes diphosphate, but not ATP, as a phosphoryl donor
additional information
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no activity with ATP
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MgCl2
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employed in assay mixture
Mn2+
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only weak activity
Mg2+
-
-
Mg2+
5 mM used in assay conditions
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ADP
80% inhibition at 1 mM
ATP
about 30% inhibition at 1 mM
additional information
not inhibited by AMP
-
additional information
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not inhibited by AMP
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0.02 - 8
acetyl phosphate
additional information
additional information
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Michaelis-Menten kinetics
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106
acetate
-
45°C, pH 7.5, wild-type
166
acetate
wild type enzyme, at pH 5.5 and 45°C
169
acetate
-
45°C, pH 7.5, mutant T223P
372
acetate
mutant enzyme Q323G/M324I, at pH 5.5 and 45°C
566
acetate
mutant enzyme Q323A/M324A, at pH 5.5 and 45°C
0.02
acetyl phosphate
pH 7.0, 37°C, recombinant enzyme
0.02
acetyl phosphate
at pH 6.0 and 37°C
0.06
acetyl phosphate
-
pH 7, 30°C
0.07
acetyl phosphate
pH 6.0, 37°C, recombinant enzyme
0.07
acetyl phosphate
at pH 6.0 and 37°C
0.34
acetyl phosphate
mutant enzyme Q323A/M324A, at pH 7.0 and 37°C
0.47
acetyl phosphate
mutant enzyme Q323G/M324I, at pH 7.0 and 37°C
0.5
acetyl phosphate
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37°C, pH 7, wild-type
0.51
acetyl phosphate
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37°C, pH 7, mutant V87G
0.53
acetyl phosphate
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37°C, pH 7, mutant V87A
0.57
acetyl phosphate
wild type enzyme, at pH 7.0 and 37°C
0.66
acetyl phosphate
mutant enzyme D272A/R274A/Q323G/M324I, at pH 7.0 and 37°C
0.69
acetyl phosphate
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37°C, pH 7, mutant H172A
1.6
acetyl phosphate
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37°C, pH 7, mutant I116A
2
acetyl phosphate
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37°C, pH 7, mutant T223P
2.4
acetyl phosphate
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37°C, pH 7, mutant I116L
8
acetyl phosphate
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37°C, pH 7, mutant H117A
56.5
Butyrate
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45°C, pH 7.5, mutant T223P
75.6
Butyrate
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45°C, pH 7.5, wild-type
1.9
diphosphate
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co-substrate: hexanoate, 45°C, pH 7.5, mutant T223P
2
diphosphate
mutant enzyme Q323G/M324I, at pH 5.5 and 45°C
2.1
diphosphate
wild type enzyme, at pH 5.5 and 45°C
2.3
diphosphate
mutant enzyme Q323A/M324A, at pH 5.5 and 45°C
3
diphosphate
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co-substrate: valerate, 45°C, pH 7.5, mutant T223P
3.2
diphosphate
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co-substrate: butyrate, 37°C, pH 7.5, wild-type
3.3
diphosphate
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pH 6.5-7.5, 30°C, recombinant enzyme
3.6
diphosphate
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co-substrate: acetyl phosphate, 37°C, pH 7.5, wild-type
4
diphosphate
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co-substrate: propionate, 45°C, pH 7.5, mutant T223P
4.8
diphosphate
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co-substrate: propionate, 37°C, pH 7.5, wild-type
4.9
diphosphate
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co-substrate: butyrate, 45°C, pH 7.5, mutant T223P
6.3
diphosphate
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co-substrate: acetate, 45°C, pH 7.5, mutant T223P
6.3
diphosphate
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co-substrate: valerate, 37°C, pH 7.5, wild-type
16.3
diphosphate
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co-substrate: hexanoate, 37°C, pH 7.5, wild-type
20.4
hexanoate
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45°C, pH 7.5, mutant T223P
20.5
hexanoate
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45°C, pH 7.5, wild-type
2.2
phosphate
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pH 7, 30°C
2.2
phosphate
pH 7.0, 37°C, recombinant enzyme
2.2
phosphate
at pH 6.0 and 37°C
2.6
phosphate
pH 6.0, 37°C, recombinant enzyme
2.6
phosphate
at pH 6.0 and 37°C
7.3
phosphate
mutant enzyme Q323G/M324I, at pH 7.0 and 37°C
8.2
phosphate
mutant enzyme Q323A/M324A, at pH 7.0 and 37°C
14
phosphate
wild type enzyme, at pH 7.0 and 37°C
18
phosphate
mutant enzyme D272A/R274A/Q323G/M324I, at pH 7.0 and 37°C
48.9
phosphate
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co-substrate: acetyl phosphate, 37°C, pH 7, wild-type
79.8
propionate
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45°C, pH 7.5, wild-type
98.7
propionate
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45°C, pH 7.5, mutant T223P
41.6
valerate
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45°C, pH 7.5, mutant T223P
56.7
valerate
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45°C, pH 7.5, wild-type
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0.052 - 8333
acetyl phosphate
0.51
acetate
mutant enzyme Q323A/M324A, at pH 5.5 and 45°C
0.51
acetate
mutant enzyme Q323G/M324I, at pH 5.5 and 45°C
1.3
acetate
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45°C, pH 7.5, mutant T223P
1.4
acetate
wild type enzyme, at pH 5.5 and 45°C
1.76
acetate
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37°C, pH 7, wild-type
0.052
acetyl phosphate
mutant enzyme D272A/R274A/Q323G/M324I, at pH 7.0 and 37°C
2
acetyl phosphate
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37°C, pH 7, mutant H172A
14
acetyl phosphate
mutant enzyme Q323A/M324A, at pH 7.0 and 37°C
21
acetyl phosphate
pH 6.0, 37°C, recombinant enzyme
21
acetyl phosphate
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37°C, pH 7, mutant H117A
21
acetyl phosphate
at pH 6.0 and 37°C
30
acetyl phosphate
pH 7.0, 37°C, recombinant enzyme
30
acetyl phosphate
at pH 7.0 and 37°C
32
acetyl phosphate
mutant enzyme Q323G/M324I, at pH 7.0 and 37°C
97
acetyl phosphate
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37°C, pH 7, mutant V87G
266
acetyl phosphate
wild type enzyme, at pH 7.0 and 37°C
280
acetyl phosphate
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37°C, pH 7, mutant I116A
344
acetyl phosphate
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37°C, pH 7, mutant I116L
1218
acetyl phosphate
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37°C, pH 7, mutant V87A
1939
acetyl phosphate
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37°C, pH 7, wild-type
8333
acetyl phosphate
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37°C, pH 7, mutant T223P
0.18
Butyrate
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45°C, pH 7.5, mutant T223P
0.33
Butyrate
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45°C, pH 7.5, wild-type
0.36
diphosphate
mutant enzyme Q323A/M324A, at pH 5.5 and 45°C
0.45
diphosphate
mutant enzyme Q323G/M324I, at pH 5.5 and 45°C
0.9
diphosphate
wild type enzyme, at pH 5.5 and 45°C
2.6
diphosphate
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pH 6.5-7.5, 30°C, recombinant enzyme
0.051
hexanoate
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45°C, pH 7.5, wild-type
0.065
hexanoate
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45°C, pH 7.5, mutant T223P
0.076
phosphate
mutant enzyme D272A/R274A/Q323G/M324I, at pH 7.0 and 37°C
2 - 8
phosphate
mutant enzyme Q323G/M324I, at pH 7.0 and 37°C
20
phosphate
mutant enzyme Q323A/M324A, at pH 7.0 and 37°C
21
phosphate
at pH 6.0 and 37°C
30
phosphate
at pH 7.0 and 37°C
196
phosphate
wild type enzyme, at pH 7.0 and 37°C
0.61
propionate
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45°C, pH 7.5, mutant T223P
1.16
propionate
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45°C, pH 7.5, wild-type
0.19
valerate
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45°C, pH 7.5, wild-type
0.21
valerate
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45°C, pH 7.5, mutant T223P
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0.08 - 3846
acetyl phosphate
0.0025 - 0.0032
hexanoate
0.0062 - 0.015
propionate
0.0009
acetate
mutant enzyme Q323A/M324A, at pH 5.5 and 45°C
0.0014
acetate
mutant enzyme Q323G/M324I, at pH 5.5 and 45°C
0.0077
acetate
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45°C, pH 7.5, mutant T223P
0.0086
acetate
wild type enzyme, at pH 5.5 and 45°C
0.016
acetate
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45°C, pH 7.5, wild-type
0.08
acetyl phosphate
mutant enzyme D272A/R274A/Q323G/M324I, at pH 7.0 and 37°C
42
acetyl phosphate
mutant enzyme Q323A/M324A, at pH 7.0 and 37°C
68
acetyl phosphate
mutant enzyme Q323G/M324I, at pH 7.0 and 37°C
300
acetyl phosphate
pH 6.0, 37°C, recombinant enzyme
355
acetyl phosphate
at pH 6.0 and 37°C
467
acetyl phosphate
wild type enzyme, at pH 7.0 and 37°C
1400
acetyl phosphate
at pH 6.0 and 37°C
1500
acetyl phosphate
pH 7.0, 37°C, recombinant enzyme
3846
acetyl phosphate
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37°C, pH 7, wild-type
0.0032
Butyrate
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45°C, pH 7.5, mutant T223P
0.0043
Butyrate
-
45°C, pH 7.5, wild-type
0.16
diphosphate
mutant enzyme Q323A/M324A, at pH 5.5 and 45°C
0.23
diphosphate
mutant enzyme Q323G/M324I, at pH 5.5 and 45°C
0.44
diphosphate
wild type enzyme, at pH 5.5 and 45°C
0.0025
hexanoate
-
45°C, pH 7.5, wild-type
0.0032
hexanoate
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45°C, pH 7.5, mutant T223P
0.004
phosphate
mutant enzyme D272A/R274A/Q323G/M324I, at pH 7.0 and 37°C
2.5
phosphate
mutant enzyme Q323A/M324A, at pH 7.0 and 37°C
3.8
phosphate
mutant enzyme Q323G/M324I, at pH 7.0 and 37°C
9
phosphate
pH 6.0, 37°C, recombinant enzyme
9
phosphate
at pH 6.0 and 37°C
12
phosphate
pH 7.0, 37°C, recombinant enzyme
12
phosphate
at pH 6.0 and 37°C
14
phosphate
wild type enzyme, at pH 7.0 and 37°C
0.0062
propionate
-
45°C, pH 7.5, mutant T223P
0.015
propionate
-
45°C, pH 7.5, wild-type
0.0034
valerate
-
45°C, pH 7.5, wild-type
0.0049
valerate
-
45°C, pH 7.5, mutant T223P
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2.4
ATP
Entamoeba histolytica
mutant enzyme D272A/R274A/Q323G/M324I, in the acetate-forming direction, at pH 7.0 and 37°C
4.2
ATP
Entamoeba histolytica
mutant enzyme Q323G/M324I, in the acetate-forming direction, at pH 7.0 and 37°C
4.8
ATP
Entamoeba histolytica
mutant enzyme Q323A/M324A, in the acetate-forming direction, at pH 7.0 and 37°C
6.1
ATP
Entamoeba histolytica
wild type enzyme, in the acetate-forming direction, at pH 7.0 and 37°C
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6
diphosphate and acetate formation reaction, assay at
6.5
-
assay at, diphosphate forming reaction direction
6.5 - 7.5
-
acetyl phosphate-forming reaction direction, assay at
7
-
assay at
7
acetyl phosphate formation reaction, assay at
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45
-
acetyl phosphate-forming direction
37
assay at
37
-
acetate-forming direction
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brenda
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brenda
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UniProt
brenda
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brenda
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UniProt
brenda
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brenda
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brenda
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brenda
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evolution
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residue Asn337 of ATP-ecoAK is particularly significant for the specificity to ATP. The five residues are highly conserved in 2625 PPi-ehiAK homologue implying that almost all organisms have ATP-dependent acetate kinase, EC 2.7.2.1, rather than diphosphate-dependent acetate kinase, EC 2.7.2.12
malfunction
AcK gene silencing does not affect acetate production in the parasites but promotes a slight decrease (10-20%) in the hexose phosphates and phosphate levels. Amoebae lacking ADP-forming acetyl-CoA synthetase activity are unable to reestablish the acetyl-CoA/CoA ratio after an oxidative stress challenge
metabolism
the enzyme does not contribute to acetate production but might be marginally involved in diphosphate and hexosephosphate homeostasis
physiological function
The enzyme does not importantly contribute to ATP and phospate supply in the amoebae. Recombinant enzyme AcK shows activity only in the acetate formation direction. Enzyme AcK does not contribute to acetate production but might be marginally involved in phosphate and hexosephosphate homeostasis
additional information
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substrate-binding site structure and comparison with ATP-dependent acetate kinase, EC 2.7.2.1, overview
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C4M1C3_ENTHI
392
0
43247
TrEMBL
-
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44000
-
x * 44000, recombinant His-tagged enzyme, SDS-PAGE
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?
-
x * 44000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
2 * 45000, His-tagged enzyme, SDS-PAGE
monomer
1 * 45000, about, sequence calculation, x * 77000, about, recombinant His6-tagged enzyme, SDS-PAGE
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D272A/R274A/Q323G/M324I
the mutations decrease kcat in the acetate-forming direction by about 2500-5000fold but have little effect on Km for either substrate compared to the wild type enzyme. This mutant has no detectable activity in the acetyl phosphate-forming direction
DELTAG203/Q323G/M324I
inactive
H117A
-
mutant is inactive in the direction of acetyl phosphate formation. In the direction of acetate formation, alteration of the His117 results in a 16fold increase in the Km for acetyl phosphate and a 95fold decreased kcat, and for a 1500fold reduction in catalytic efficiency
H172A
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mutant is inactive in the direction of acetyl phosphate formation. The His172Ala mutant has a similar Km for acetyl phosphate as wild-type, the kcat value is reduced 970fold
I116A
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mutant shows no substantial change in the Km for acetate, mutant has a 26fold decreased kcat. In the direction of acetate formation, the Ile116Ala and Ile116Leu variants both display a mild increase in the Km for acetyl phosphate and decreased kcat, resulting in 22- to 27fold-decreased catalytic efficiencies, respectively
I116L
-
mutant shows no substantial change in the Km for acetate. In the direction of acetate formation, the Ile116Ala and Ile116Leu variants both display a mild increase in the Km for acetyl phosphate and decreased kcat, resulting in 22- to 27fold-decreased catalytic efficiencies, respectively
Q323A/M324A
the variant displays similar Km values for acetyl phosphate and slightly decreased Km values for phosphate as the wild type enzyme but the kcat value is decreased 19fold resulting in about 11fold reduced catalytic efficiency. In the direction of acetyl phosphate formation, these variant displays slightly increased Km for acetate but no increase in Km for diphosphate and only mild decrease in kcat
Q323G/M324I
the variant displays similar Km values for acetyl phosphate and slightly decreased Km values for phosphate as the wild type enzyme but the kcat value is decreased 8.3fold resulting in about 7fold reduced catalytic efficiency. In the direction of acetyl phosphate formation, these variant displays slightly increased Km for acetate but no increase in Km for diphosphate and only mild decrease in kcat
T223G
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mutant shows significant activity in the acetate-forming direction of the assay but does not display activity in the acyl phosphate-forming direction with any acyl substrate
T223P
-
mutant shows little effect on enzyme activity in the direction of acyl phosphate formation. The enzyme remains capable of utilizing substrates as long as hexanoate, and the Km and kcat values for each substrate are comparable to wild-type. In the direction of acetate formation, the Km for acetyl phosphate increases 4fold, the kcat also shows a 4fold increase, and thus the catalytic efficiency, kcat/Km, is unchanged
V87A
-
mutant displays 16- to 20fold decreased turnover rates in the direction of acetate synthesis but no change in the Km for acetyl phosphate, and they are inactive in the acetyl phosphate-forming direction
V87G
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mutant displays 16- to 20fold decreased turnover rates in the direction of acetate synthesis but no change in the Km for acetyl phosphate, and they are inactive in the acetyl phosphate-forming direction
additional information
constructio of an acetate kinase antisense knockout mutant strain
additional information
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constructio of an acetate kinase antisense knockout mutant strain
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4°C, under N2, stable for a week
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Co2+ affinity column chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography
using Ni-NTA chromatography
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-
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expressed in Escherichia coli as a His-tagged fusion protein
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expressed in Escherichia coli YBS121 DELTAack DELTApta cells
gene CL6EHI_170010, DNA and amino acid sequence determination and analysis, quantitative expression analysis by qRT-PCR, recombinant overexpression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
sequence comparisons, recombinant overexpression of His-tagged enzyme in Escherichia coli strain MK3648
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Reeves, R.; Guthrie, J.D.
Acetate kinase (pyrophosphate). A fourth pyrophosphate-dependent kinase from Entamoeba histolytica
Biochem. Biophys. Res. Commun.
66
1389-1395
1975
Entamoeba histolytica, Entamoeba histolytica H200
brenda
Fowler, M.L.; Ingram-Smith, C.; Smith, K.S.
Novel pyrophosphate-forming acetate kinase from the protist Entamoeba histolytica
Eukaryot. Cell
11
1249-1256
2012
Entamoeba histolytica
brenda
Pineda, E.; Vazquez, C.; Encalada, R.; Nozaki, T.; Sato, E.; Hanadate, Y.; Nequiz, M.; Olivos-Garcia, A.; Moreno-Sanchez, R.; Saavedra, E.
Roles of acetyl-CoA synthetase (ADP-forming) and acetate kinase (PPi-forming) in ATP and PPi supply in Entamoeba histolytica
Biochim. Biophys. Acta
1860
1163-1172
2016
Entamoeba histolytica (C4M1C3), Entamoeba histolytica
brenda
Yoshioka, A.; Murata, K.; Kawai, S.
Structural and mutational analysis of amino acid residues involved in ATP specificity of Escherichia coli acetate kinase
J. Biosci. Bioeng.
118
502-507
2014
Entamoeba histolytica
brenda
Pineda, E.; Vazquez, C.; Encalada, R.; Nozaki, T.; Sato, E.; Hanadate, Y.; Nequiz, M.; Olivos-Garcia, A.; Moreno-Sanchez, R.; Saavedra, E.
Roles of acetyl-CoA synthetase (ADP-forming) and acetate kinase (PPi-forming) in ATP and PPi supply in Entamoeba histolytica
Biochim. Biophys. Acta
1860
1163-1172
2016
Entamoeba histolytica (C4M1C3), Entamoeba histolytica
brenda
Dang, T.; Ingram-Smith, C.
Investigation of pyrophosphate versus ATP substrate selection in the Entamoeba histolytica acetate kinase
Sci. Rep.
7
5912
2017
Entamoeba histolytica (C4M1C3), Entamoeba histolytica
brenda
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